There's a number of articles (some of which are written by my ex-boss) on
the subject. It seems that not everything is solubilized equally, and not
all fusion partners are equal. MBP seems to not only solubilize, but also
partially improve folding, for instance.
One of the ideas is that the fastest-folded fusion partner sequesters the
unfolded polypeptide chain of the other fusion partner and thus prevents
these unfolded chains from crosslinking. Given time, these chains become
ordered. There's a number of other theories too :)
A.G.E.
"Emir Khatipov" <khatipovNO at NOuchicago.edu> wrote in message
news:dtMh8.43$s4.2500 at news.uchicago.edu...
> Is that known why thioredoxin, GST stabilize otherwise insoluble proteins
> when expressed in fusion? Could that be due to changes in conformation of
> the fusion partner? Is stabilization related to redox properties of Trx
and
> GST, and how? Protection of disulfides that hold the structure together or
> anything else? What's the general dogma?
>> Any leads and discussion will be much appreciated.
>> Emir
>>